English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  The tetragonal surface layer of Clostridium aceticum: three-dimensional structure and comparison with the hexagonal layer of Clostridium thermohydrosulfuricum

Woodcock, C. L., Engelhardt, H., & Baumeister, W. (1986). The tetragonal surface layer of Clostridium aceticum: three-dimensional structure and comparison with the hexagonal layer of Clostridium thermohydrosulfuricum. European Journal of Cell Biology., 42(2), 211-217.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Woodcock, C. L., Author
Engelhardt, H.1, Author           
Baumeister, W.1, Author           
Affiliations:
1External Organizations, ou_persistent22              

Content

show
hide
Free keywords: Bacterial Proteins; *Clostridium/ul [Ultrastructure]; Comparative Study; Computer Simulation; Evolution; Macromolecular Systems; Species Specificity
 Abstract: The regular surface layer (S-layer) of Clostridium aceticum has been isolated and the three-dimensional structure determined to a resolution of 2.0 nm from tilt series of negatively stained preparations. It has tetragonal symmetry with a lattice constant of 12 nm and a thickness of 6 nm; there are probably 4 protein monomers per unit cell. A large proportion of the protein is concentrated in massive "cores" at the major four-fold axes which are situated towards the inner surface of the layer. From these cores, delicate arms extend towards the minor four-fold axes, where secondary connectivity is established near the exterior surface. When viewed from the outside, each of the cores appears to have a large central depression, rather than a true "pore". Since this general pattern of mass distribution is shared by the hexagonal S-layer of Clostridium thermohydrosulfuricum, some consideration has been given to the possible evolutionary steps leading to changes in symmetry. From modelling experiments, it is evident that the change from four-fold to six-fold symmetry in this instance could be accomplished simply by the loss of a structural "domain" from the protomer.

Details

show
hide
Language(s):
 Dates: 1986
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 318749
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: European Journal of Cell Biology.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 42 (2) Sequence Number: - Start / End Page: 211 - 217 Identifier: -